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Conserved domains on  [gi|20544160|ref|NP_620550|]
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fumble, isoform A [Drosophila melanogaster]

Protein Classification

type II pantothenate kinase( domain architecture ID 10508179)

type II pantothenate kinase catalyzes the formation of (R)-4'-phosphopantothenate from (R)-pantothenate in coenzyme A biosynthesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ASKHA_NBD_PanK-II_Pank1-like cd24122
nucleotide-binding domain (NBD) of the pantothenate kinase 1 (Pank1)-like subfamily; PanK (EC ...
21-369 0e+00

nucleotide-binding domain (NBD) of the pantothenate kinase 1 (Pank1)-like subfamily; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. Eukaryotic PanK-II enzymes often occur as different isoforms, such as PanK1, PanK2, PanK3 and PanK4. The Pank1-like subfamily includes PanK1-3.


:

Pssm-ID: 466972 [Multi-domain]  Cd Length: 303  Bit Score: 562.14  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160  21 WFGMDIGGTLTKLVYFEPKditpdeqdreagilrnirryltknsaygktghrdthlqmdnveirkrrGSLHFIRFQTTDM 100
Cdd:cd24122   1 WFGLDIGGTLVKLVYFEPT------------------------------------------------GTLHFIRFETSRM 32
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 101 GNFLSLAKQKGMAELVTTVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFADLHNRTECYYYENARDILKSEK- 179
Cdd:cd24122  33 EGFIQLAREKNLSSLIKTVCATGGGAYKFEKLFREELGLQLHKLDELDCLIRGINFLLRHVPDECYYFENPSDPELCEKr 112
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 180 -QQFNFSQPFPFILVNVGSGVSILAVYGPDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKDI 258
Cdd:cd24122 113 vVPFDFSDPYPYLLVNIGSGVSILAVESPDNYERVSGTSLGGGTFLGLCCLLTGCETFEEALELAAKGDSTKVDMLVGDI 192
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 259 YGGDYNRFGLPGDLVASSFGQMHLNDKRVSVSREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNPISMKL 338
Cdd:cd24122 193 YGGDYEKFGLPGDTVASSFGKMVAKEKRESASKEDLARALLVMITNNIGSIARLCAKNEGIKRVVFVGNFLRHNPIAMRL 272
                       330       340       350
                ....*....|....*....|....*....|.
gi 20544160 339 LAYAMEFWSNGTMKGLFLEHEGYFGALGCLL 369
Cdd:cd24122 273 LAYAMDYWSKGEMKALFLEHEGYFGALGALL 303
 
Name Accession Description Interval E-value
ASKHA_NBD_PanK-II_Pank1-like cd24122
nucleotide-binding domain (NBD) of the pantothenate kinase 1 (Pank1)-like subfamily; PanK (EC ...
21-369 0e+00

nucleotide-binding domain (NBD) of the pantothenate kinase 1 (Pank1)-like subfamily; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. Eukaryotic PanK-II enzymes often occur as different isoforms, such as PanK1, PanK2, PanK3 and PanK4. The Pank1-like subfamily includes PanK1-3.


Pssm-ID: 466972 [Multi-domain]  Cd Length: 303  Bit Score: 562.14  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160  21 WFGMDIGGTLTKLVYFEPKditpdeqdreagilrnirryltknsaygktghrdthlqmdnveirkrrGSLHFIRFQTTDM 100
Cdd:cd24122   1 WFGLDIGGTLVKLVYFEPT------------------------------------------------GTLHFIRFETSRM 32
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 101 GNFLSLAKQKGMAELVTTVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFADLHNRTECYYYENARDILKSEK- 179
Cdd:cd24122  33 EGFIQLAREKNLSSLIKTVCATGGGAYKFEKLFREELGLQLHKLDELDCLIRGINFLLRHVPDECYYFENPSDPELCEKr 112
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 180 -QQFNFSQPFPFILVNVGSGVSILAVYGPDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKDI 258
Cdd:cd24122 113 vVPFDFSDPYPYLLVNIGSGVSILAVESPDNYERVSGTSLGGGTFLGLCCLLTGCETFEEALELAAKGDSTKVDMLVGDI 192
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 259 YGGDYNRFGLPGDLVASSFGQMHLNDKRVSVSREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNPISMKL 338
Cdd:cd24122 193 YGGDYEKFGLPGDTVASSFGKMVAKEKRESASKEDLARALLVMITNNIGSIARLCAKNEGIKRVVFVGNFLRHNPIAMRL 272
                       330       340       350
                ....*....|....*....|....*....|.
gi 20544160 339 LAYAMEFWSNGTMKGLFLEHEGYFGALGCLL 369
Cdd:cd24122 273 LAYAMDYWSKGEMKALFLEHEGYFGALGALL 303
Fumble pfam03630
Fumble; Fumble is required for cell division in Drosophila. Mutants lacking fumble exhibit ...
22-367 2.03e-167

Fumble; Fumble is required for cell division in Drosophila. Mutants lacking fumble exhibit abnormalities in bipolar spindle organization, chromosome segregation, and contractile ring formation. Analyses have demonstrated that encodes three protein isoforms, all of which contain a domain with high similarity to the pantothenate kinases of A. nidulans and mouse. A role of fumble in membrane synthesis has been proposed.


Pssm-ID: 460995 [Multi-domain]  Cd Length: 311  Bit Score: 471.59  E-value: 2.03e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160    22 FGMDIGGTLTKLVYFEPKDITPDEQDreagilrnirryltknsaygktghrdthlqmdnveirkrrGSLHFIRFQTTDMG 101
Cdd:pfam03630   1 FAIDIGGTLAKLVYFSPVPDSPKELG----------------------------------------GRLHFIKFETTKIE 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160   102 NFLSLAKQKGMAELVT----TVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFADLHNRTECYYYENARdilKS 177
Cdd:pfam03630  41 DCLEFIKSLGLNSKGTdrglTVKATGGGAYKFYDLFKEKLGVKVDKEDEMECLIKGLNFLLTNIPDEVFTYSDSP---EY 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160   178 EKQQFNFSQPFPFILVNVGSGVSILAVYGPDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKD 257
Cdd:pfam03630 118 FFQTVDNNSIYPYLLVNIGSGVSILKVEGPDKFERVGGTSLGGGTFWGLCSLLTGAKSFDEMLELAEKGDNRNVDMLVGD 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160   258 IYGGDYNRFGLPGDLVASSFGQMHLNDKRVSV----SREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNP 333
Cdd:pfam03630 198 IYGGDYEKIGLKSDTIASSFGKVFRKKFRESAsndaSPEDIARSLLYMISNNIGQIAYLNAKLHGLKRIYFGGNFIRGHP 277
                         330       340       350
                  ....*....|....*....|....*....|....
gi 20544160   334 ISMKLLAYAMEFWSNGTMKGLFLEHEGYFGALGC 367
Cdd:pfam03630 278 ITMKTLSYAINFWSKGELKALFLRHEGYLGALGA 311
panK_eukar TIGR00555
pantothenate kinase, eukaryotic/staphyloccocal type; This model describes a eukaryotic form of ...
20-369 7.76e-110

pantothenate kinase, eukaryotic/staphyloccocal type; This model describes a eukaryotic form of pantothenate kinase, characterized from the fungus Aspergillus nidulans and with similar forms known in several other eukaryotes. It also includes forms from several Gram-positive bacteria suggested to have originated from the eukaryotic form by lateral transfer. It differs in a number of biochemical properties (such as inhibition by acetyl-CoA) from most bacterial CoaA and lacks sequence similarity. This enzyme is the key regulatory step in the biosynthesis of coenzyme A (CoA). [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 273135 [Multi-domain]  Cd Length: 296  Bit Score: 324.74  E-value: 7.76e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160    20 PWFGMDIGGTLTKLVYFEPKditpdeqdreagilrnirryltknsaygktghrdthlqmdnveirkrrGSLHFIRFQTTD 99
Cdd:TIGR00555   1 SRIGIDIGGTLIKVVYEEKK------------------------------------------------GRRKFKTFETTN 32
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160   100 MGNFLSLAK-QKGMAELVTTVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFADLHNRTECYYYENArdilKSE 178
Cdd:TIGR00555  33 IDKFIEWLKnQIHRHSRITTLCATGGGAFKFAELIYESAGIQLHKFDEFDALIQGLNYLLKEEPKEKFTYYDF----ECQ 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160   179 KQQFNFSQPFPFILVNVGSGVSILAVYGpDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKDI 258
Cdd:TIGR00555 109 KKPIDLDDIYPYLLVNIGTGTSILYVDG-DNYERVGGTSLGGGTFLGLGKLLTGIQTFDELLEMAQHGDRTNVDLLVGDI 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160   259 YGGDYNRFGLPGDLVASSFGQMHLNDKRVSVSREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNPISMKL 338
Cdd:TIGR00555 188 YGGDYSESGLDGSLTASSFGKVLSKHLDQSFSPEDIAASLLGLIGNNIGQIAYLCALRYNIDRIVFIGSFLRNNQLLMKV 267
                         330       340       350
                  ....*....|....*....|....*....|.
gi 20544160   339 LAYAMEFWSngtMKGLFLEHEGYFGALGCLL 369
Cdd:TIGR00555 268 LSYATNFWS---KKALFLEHEGYSGAIGALL 295
PLN02902 PLN02902
pantothenate kinase
22-372 4.34e-69

pantothenate kinase


Pssm-ID: 215489 [Multi-domain]  Cd Length: 876  Bit Score: 234.40  E-value: 4.34e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160   22 FGMDIGGTLTKLVYFEPKDITPDEQDREagilRNIRRYLTKNSaygktGHRDTHLQMDnveirkrrGSLHFIRFQTTDMG 101
Cdd:PLN02902  56 LALDIGGSLIKLVYFSRHEDRSTDDKRK----RTIKERLGITN-----GNRRSYPILG--------GRLHFVKFETSKIN 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160  102 NFLSLAKQKGM-------------AELVTTVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFADLHNRTECYYY 168
Cdd:PLN02902 119 ECLDFISSKQLhrggihswlskapPNGNGVIKATGGGAYKFADLFKERLGVSLDKEDEMDCLVAGANFLLKAIRHEAFTH 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160  169 enardiLKSEKQ--QFNFSQPFPFILVNVGSGVSILAVYGPDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKG 246
Cdd:PLN02902 199 ------MEGEKEfvQIDQNDLFPYLLVNIGSGVSMIKVDGDGKFERVSGTNVGGGTYWGLGRLLTKCKSFDELLELSQRG 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160  247 DNRKVDKLVKDIYGG-DYNRFGLPGDLVASSFGQMHLNDKRVSVSR-EDLANATLVTITNNIGSIARMCALNEKIDRVVF 324
Cdd:PLN02902 273 DNSAIDMLVGDIYGGmDYSKIGLSASTIASSFGKVISENKELSDYRpEDISLSLLRMISYNIGQISYLNALRFGLKRIFF 352
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 20544160  325 VGNFLRVNPISMKLLAYAMEFWSNGTMKGLFLEHEGYFGALGCLLQFN 372
Cdd:PLN02902 353 GGFFIRGHAYTMDTISFAVHFWSKGEAQAMFLRHEGFLGALGAFMSYE 400
PanK COG5146
Pantothenate kinase [Coenzyme transport and metabolism]; Pantothenate kinase is part of the ...
23-369 1.27e-40

Pantothenate kinase [Coenzyme transport and metabolism]; Pantothenate kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 444059 [Multi-domain]  Cd Length: 270  Bit Score: 145.42  E-value: 1.27e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160  23 GMDIGGTLTKLVYFEpkditpdeqdreagilrnirryltknsaygktghrdthlqmdnveirkrRGSLHFIRFQTTDMGN 102
Cdd:COG5146   5 GIDAGGTLTKIAYLE-------------------------------------------------DGERRYKKFPSDEIES 35
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 103 FLS-LAKQKGMAElvttVCATGGGAFKFEQDFRDqvnMKLAKFDELDTLIKGILFadlhnrtecyyyenardILKSEKQQ 181
Cdd:COG5146  36 VADwLNKFINIEK----IGLTGGRAEVLAEKLNG---DPKQYIVEFDATGKGVRY-----------------LLKEEGHD 91
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 182 FNfsqpfPFILVNVGSGVSILAVYGpDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKDIYGG 261
Cdd:COG5146  92 ID-----KFIITNVGTGTSIHYMDG-DTQERVGGTGVGGGTLMGLSYLLTGISDFEEIVELAKKGDRDGIDLKVKDIYEG 165
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 262 DYNrfGLPGDLVASSFGQMHLNDKRvSVSREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNPismkLLAY 341
Cdd:COG5146 166 MEP--PIPGDLTASNFGKVLITLDE-SATKEDILAAIIGLVGETITTLSIQAAEEYDTETIVYIGSTLTNNP----LLQE 238
                       330       340       350
                ....*....|....*....|....*....|.
gi 20544160 342 AMEFWSngTMKGL---FLEHEGYFGALGCLL 369
Cdd:COG5146 239 VIESYT--ILRGKkpiFLENGEFSGAIGALL 267
 
Name Accession Description Interval E-value
ASKHA_NBD_PanK-II_Pank1-like cd24122
nucleotide-binding domain (NBD) of the pantothenate kinase 1 (Pank1)-like subfamily; PanK (EC ...
21-369 0e+00

nucleotide-binding domain (NBD) of the pantothenate kinase 1 (Pank1)-like subfamily; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. Eukaryotic PanK-II enzymes often occur as different isoforms, such as PanK1, PanK2, PanK3 and PanK4. The Pank1-like subfamily includes PanK1-3.


Pssm-ID: 466972 [Multi-domain]  Cd Length: 303  Bit Score: 562.14  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160  21 WFGMDIGGTLTKLVYFEPKditpdeqdreagilrnirryltknsaygktghrdthlqmdnveirkrrGSLHFIRFQTTDM 100
Cdd:cd24122   1 WFGLDIGGTLVKLVYFEPT------------------------------------------------GTLHFIRFETSRM 32
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 101 GNFLSLAKQKGMAELVTTVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFADLHNRTECYYYENARDILKSEK- 179
Cdd:cd24122  33 EGFIQLAREKNLSSLIKTVCATGGGAYKFEKLFREELGLQLHKLDELDCLIRGINFLLRHVPDECYYFENPSDPELCEKr 112
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 180 -QQFNFSQPFPFILVNVGSGVSILAVYGPDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKDI 258
Cdd:cd24122 113 vVPFDFSDPYPYLLVNIGSGVSILAVESPDNYERVSGTSLGGGTFLGLCCLLTGCETFEEALELAAKGDSTKVDMLVGDI 192
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 259 YGGDYNRFGLPGDLVASSFGQMHLNDKRVSVSREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNPISMKL 338
Cdd:cd24122 193 YGGDYEKFGLPGDTVASSFGKMVAKEKRESASKEDLARALLVMITNNIGSIARLCAKNEGIKRVVFVGNFLRHNPIAMRL 272
                       330       340       350
                ....*....|....*....|....*....|.
gi 20544160 339 LAYAMEFWSNGTMKGLFLEHEGYFGALGCLL 369
Cdd:cd24122 273 LAYAMDYWSKGEMKALFLEHEGYFGALGALL 303
ASKHA_NBD_PanK-II_Pank1 cd24135
nucleotide-binding domain (NBD) of pantothenate kinase 1 (Pank1) from type II pantothenate ...
21-369 9.70e-180

nucleotide-binding domain (NBD) of pantothenate kinase 1 (Pank1) from type II pantothenate kinase (PanK-II) subfamily; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. Eukaryotic PanK-II enzymes often occur as different isoforms, such as PanK1, PanK2, PanK3 and PanK4. The model corresponds to PanK1.


Pssm-ID: 466985 [Multi-domain]  Cd Length: 352  Bit Score: 504.53  E-value: 9.70e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160  21 WFGMDIGGTLTKLVYFEPKDITPDEQDREAGILRNIRRYLTKNSAYGKTGHRDTHLQMDNVEIRKRRGSLHFIRFQTTDM 100
Cdd:cd24135   1 WFGMDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPSCAM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 101 GNFLSLAKQKGMAELVTTVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFAD---LHNRTECYYYENARDILKS 177
Cdd:cd24135  81 HRFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDsvgFNGQPECYYFENPTDPEQC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 178 EKQQFNFSQPFPFILVNVGSGVSILAVYGPDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKD 257
Cdd:cd24135 161 QKKPYCLDNPYPMLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVKD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 258 IYGGDYNRFGLPGDLVASSFGQMHLNDKRVSVSREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNPISMK 337
Cdd:cd24135 241 IYGGDYERFGLQGSAVASSFGHMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMK 320
                       330       340       350
                ....*....|....*....|....*....|..
gi 20544160 338 LLAYAMEFWSNGTMKGLFLEHEGYFGALGCLL 369
Cdd:cd24135 321 LLAYAMDFWSKGQLKALFLEHEGYFGAVGALL 352
ASKHA_NBD_PanK-II_Pank2 cd24136
nucleotide-binding domain (NBD) of pantothenate kinase 2 (Pank2) from type II pantothenate ...
21-371 2.74e-179

nucleotide-binding domain (NBD) of pantothenate kinase 2 (Pank2) from type II pantothenate kinase (PanK-II) subfamily; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. Eukaryotic PanK-II enzymes often occur as different isoforms, such as PanK1, PanK2, PanK3 and PanK4. The model corresponds to PanK2.


Pssm-ID: 466986 [Multi-domain]  Cd Length: 354  Bit Score: 503.76  E-value: 2.74e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160  21 WFGMDIGGTLTKLVYFEPKDITPDEQDREAGILRNIRRYLTKNSAYGKTGHRDTHLQMDNVEIRKRRGSLHFIRFQTTDM 100
Cdd:cd24136   1 WFGLDIGGTLVKLVYFEPKDITAEEEEEEVENLKSIRKYLTSNVAYGSTGIRDVHLELKDLTLCGRKGNLHFIRFPTHDM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 101 GNFLSLAKQKGMAELVTTVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFAD---LHNRTECYYYENARDILKS 177
Cdd:cd24136  81 PAFIQMGRDKHFSSLHTTLCATGGGAYKFEQDFLTMGDLQLCKLDELDCLIKGVLYIDsvgFNGHSECYYFENPTDSEKC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 178 EKQQFNFSQPFPFILVNVGSGVSILAVYGPDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKD 257
Cdd:cd24136 161 QKLPFNLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGTSLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 258 IYGGDYNRFGLPGDLVASSFGQMHLNDKRVSVSREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNPISMK 337
Cdd:cd24136 241 IYGGDYERFGLPGWAVASSFGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINRVVFVGNFLRINTISMR 320
                       330       340       350
                ....*....|....*....|....*....|....
gi 20544160 338 LLAYAMEFWSNGTMKGLFLEHEGYFGALGCLLQF 371
Cdd:cd24136 321 LLAYALDYWSKGQLKALFLEHEGYFGAVGALLEL 354
Fumble pfam03630
Fumble; Fumble is required for cell division in Drosophila. Mutants lacking fumble exhibit ...
22-367 2.03e-167

Fumble; Fumble is required for cell division in Drosophila. Mutants lacking fumble exhibit abnormalities in bipolar spindle organization, chromosome segregation, and contractile ring formation. Analyses have demonstrated that encodes three protein isoforms, all of which contain a domain with high similarity to the pantothenate kinases of A. nidulans and mouse. A role of fumble in membrane synthesis has been proposed.


Pssm-ID: 460995 [Multi-domain]  Cd Length: 311  Bit Score: 471.59  E-value: 2.03e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160    22 FGMDIGGTLTKLVYFEPKDITPDEQDreagilrnirryltknsaygktghrdthlqmdnveirkrrGSLHFIRFQTTDMG 101
Cdd:pfam03630   1 FAIDIGGTLAKLVYFSPVPDSPKELG----------------------------------------GRLHFIKFETTKIE 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160   102 NFLSLAKQKGMAELVT----TVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFADLHNRTECYYYENARdilKS 177
Cdd:pfam03630  41 DCLEFIKSLGLNSKGTdrglTVKATGGGAYKFYDLFKEKLGVKVDKEDEMECLIKGLNFLLTNIPDEVFTYSDSP---EY 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160   178 EKQQFNFSQPFPFILVNVGSGVSILAVYGPDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKD 257
Cdd:pfam03630 118 FFQTVDNNSIYPYLLVNIGSGVSILKVEGPDKFERVGGTSLGGGTFWGLCSLLTGAKSFDEMLELAEKGDNRNVDMLVGD 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160   258 IYGGDYNRFGLPGDLVASSFGQMHLNDKRVSV----SREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNP 333
Cdd:pfam03630 198 IYGGDYEKIGLKSDTIASSFGKVFRKKFRESAsndaSPEDIARSLLYMISNNIGQIAYLNAKLHGLKRIYFGGNFIRGHP 277
                         330       340       350
                  ....*....|....*....|....*....|....
gi 20544160   334 ISMKLLAYAMEFWSNGTMKGLFLEHEGYFGALGC 367
Cdd:pfam03630 278 ITMKTLSYAINFWSKGELKALFLRHEGYLGALGA 311
ASKHA_NBD_PanK-II_Pank3 cd24137
nucleotide-binding domain (NBD) of pantothenate kinase 3 (Pank3) from type II pantothenate ...
21-369 1.05e-162

nucleotide-binding domain (NBD) of pantothenate kinase 3 (Pank3) from type II pantothenate kinase (PanK-II) subfamily; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. Eukaryotic PanK-II enzymes often occur as different isoforms, such as PanK1, PanK2, PanK3 and PanK4. The model corresponds to PanK3.


Pssm-ID: 466987 [Multi-domain]  Cd Length: 353  Bit Score: 461.40  E-value: 1.05e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160  21 WFGMDIGGTLTKLVYFEPKDITPDEQDREAGILRNIRRYLTKNSAYGKTGHRDTHLQMDNVEIRKRRGSLHFIRFQTTDM 100
Cdd:cd24137   1 WFGMDIGGTLVKLSYFEPIDITAEEEQEEVESLKSIRKYLTSNVAYGSTGIRDVHLELKDLTLFGRRGNLHFIRFPTQDL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 101 GNFLSLAKQKGMAELVTTVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFAD---LHNRTECYYYENARDILKS 177
Cdd:cd24137  81 PTFIQMGRDKNFSTLQTVLCATGGGAYKFEKDFRTIGNLHLHKLDELDCLVKGLLYIDsvsFNGQAECYYFANASEPERC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 178 EKQQFNFSQPFPFILVNVGSGVSILAVYGPDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKD 257
Cdd:cd24137 161 QKMPFNLDDPYPLLVVNIGSGVSILAVHSKDNYKRVTGTSLGGGTFLGLCSLLTGCESFEEALEMASKGDSTQADKLVRD 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 258 IYGGDYNRFGLPGDLVASSFGQMHLNDKRVSVSREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNPISMK 337
Cdd:cd24137 241 IYGGDYERFGLPGWAVASSFGNMIYKEKRESVSKEDLARATLVTITNNIGSVARMCAVNEKINRVVFVGNFLRVNTLSMK 320
                       330       340       350
                ....*....|....*....|....*....|..
gi 20544160 338 LLAYAMEFWSNGTMKGLFLEHEGYFGALGCLL 369
Cdd:cd24137 321 LLAYALDYWSKGQLKALFLEHEGYFGAVGALL 352
ASKHA_NBD_PanK-II cd24016
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins; ...
21-369 4.80e-134

nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. Eukaryotic PanK-II enzymes often occur as different isoforms, such as PanK1, PanK2, PanK3 and PanK4. The model corresponds to PanK-II that belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466866 [Multi-domain]  Cd Length: 299  Bit Score: 386.62  E-value: 4.80e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160  21 WFGMDIGGTLTKLVYFepkditpdeqdreagilrnirryltknsaygktghrdthlqmdnveirkrrgsLHFIRFQTTDM 100
Cdd:cd24016   1 WFGIDIGGTLVKLVYF-----------------------------------------------------LHFIRFPTDQV 27
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 101 GNFLSLAKQKGMAELVTTVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFAD---LHNRTECYYYENARDILKS 177
Cdd:cd24016  28 VEFIQMGQDKNFSTLITKLCATGGGAGKFEEDFRTIGNLPLQKLDELDCLSQGLLYLDsvqFNGQAECYYFANASEPERC 107
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 178 EKQQFNFSQPFPFILVNVGSGVSILAVYGPDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKD 257
Cdd:cd24016 108 QKMPFNLHDPYPYLFVNVGSGVSILAVDSKDNYKRVTGTSLGGGTFQGLCYLLTGCTDFEEALEMAQHGDSTTIDKLVRD 187
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 258 IYGGDYNRFGLPGDLVASSFGQMHLNDKRVSVSREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNPISMK 337
Cdd:cd24016 188 IYGGDYERFGLPGDAVASSFGNMLHKEKRADFSKEDLARATLGTITNNIGSMARMCARNEKIENVVFVGNFLRNNALLMK 267
                       330       340       350
                ....*....|....*....|....*....|..
gi 20544160 338 LLAYAMEFWSNGTMKGLFLEHEGYFGALGCLL 369
Cdd:cd24016 268 LLAYATDLWSKGQLKALFVEHEGYFGAVGALL 299
ASKHA_NBD_PanK-II_euk cd24086
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins ...
21-369 5.41e-126

nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins mainly from eukaryotes; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. The model corresponds to a group of PanK-II that is mainly from eukaryotes. Eukaryotic PanK-II enzymes often occur as different isoforms, such as PanK1, PanK2, PanK3 and PanK4.


Pssm-ID: 466936 [Multi-domain]  Cd Length: 327  Bit Score: 367.38  E-value: 5.41e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160  21 WFGMDIGGTLTKLVYFEPKDIT--PDEQDREAGILRNIRRYltknsaygktghrdthlqmdnveirkrrGSLHFIRFQTT 98
Cdd:cd24086   1 RLGLDIGGTLAKLAYLTPIDIDeaEEKESVLLKLLANSGED----------------------------GELHFISFPNK 52
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160  99 DMGNFLSLAKQKGMAEL--VTTVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFADLHN-RTECYYYENARDIL 175
Cdd:cd24086  53 DLEEFLNFLRDKNFEDSskGKVLYATGGGAYKYAELIEETLGVQLVKVDEMDSLVNGLHFLLSVLsKDECFPFPNDSGPE 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 176 KSEKQQFNFSQPFPFILVNVGSGVSILAVYGPDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLV 255
Cdd:cd24086 133 FLQKDPQLSDDLFPCLLVNIGSGVSILKVDSDGKYERVSGTSLGGGTFLGLASLLTGTNSFDELLELASRGDRANVDLLV 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 256 KDIYGGDYNRFGLPGDLVASSFGQM-HLNDKRVSVSREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNPI 334
Cdd:cd24086 213 RDIYGGDYPYLGLPGDLLASSFGKLaDDEKSREDFSKEDIARSLLRMIVNNIGYLAYLVAKLHNVKRVFFTGNFIRNNEL 292
                       330       340       350
                ....*....|....*....|....*....|....*
gi 20544160 335 SMKLLAYAMEFWSNGTMKGLFLEHEGYFGALGCLL 369
Cdd:cd24086 293 ARKLIAEALNYWSKGSLNALFLRHDGYLGALGALL 327
ASKHA_NBD_PanK-II_Pank4 cd24123
nucleotide-binding domain (NBD) of pantothenate kinase 4 (Pank4) from type II pantothenate ...
22-369 6.57e-113

nucleotide-binding domain (NBD) of pantothenate kinase 4 (Pank4) from type II pantothenate kinase (PanK-II) subfamily; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. Eukaryotic PanK-II enzymes often occur as different isoforms, such as PanK1, PanK2, PanK3 and PanK4. The model corresponds to PanK4, which is a putative bifunctional protein with a predicted amino-terminal pantothenate kinase (type II PanK) domain fused to a carboxy-terminal phosphatase domain. PanK4 homologs are found in animals, fungi, and plants. The human PanK4 kinase domain has catalytically-inactivating amino acid substitutions, thus it is characterized as a catalytically inactive pseudoPanK.


Pssm-ID: 466973 [Multi-domain]  Cd Length: 339  Bit Score: 334.14  E-value: 6.57e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160  22 FGMDIGGTLTKLVYFEP-KDITPDEQDREAGILRNIRRYLTKNSAYGKTGHRdthlqmdnveirkrrgsLHFIRFQTTDM 100
Cdd:cd24123   2 FAIDIGGSLAKLVYFSRvSDKAASVSSSSGTSKGPSDEPLYEVSEQPELGGR-----------------LHFVKFETKYI 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 101 GNFLSLAKQKGMAELV-----TTVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFADLHNRTECYYYEnardil 175
Cdd:cd24123  65 EECLDFIKDNLLHSRQgnkrgKVIKATGGGAYKYADLIKEKLGVEVDKEDEMECLIKGCNFLLKNIPDEVFTYD------ 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 176 KSEKQQFNF----SQPFPFILVNVGSGVSILAVYGPDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKV 251
Cdd:cd24123 139 EHAKPEVKFqsdpPDIFPYLLVNIGSGVSILKVDSEDKFERVGGTSLGGGTFWGLGSLLTGAKSFDELLELAEKGDNRNV 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 252 DKLVKDIYGGDYNRFGLPGDLVASSFG---QMHLNDKRVSVSREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNF 328
Cdd:cd24123 219 DMLVGDIYGGDYSKIGLKSDTIASSFGkvaRADKDARLEDFSPEDIAKSLLRMISNNIGQIAYLNAKLHGLKRIYFGGFF 298
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 20544160 329 LRVNPISMKLLAYAMEFWSNGTMKGLFLEHEGYFGALGCLL 369
Cdd:cd24123 299 IRGHPLTMHTISYAINFWSKGEMQALFLRHEGYLGAIGAFL 339
panK_eukar TIGR00555
pantothenate kinase, eukaryotic/staphyloccocal type; This model describes a eukaryotic form of ...
20-369 7.76e-110

pantothenate kinase, eukaryotic/staphyloccocal type; This model describes a eukaryotic form of pantothenate kinase, characterized from the fungus Aspergillus nidulans and with similar forms known in several other eukaryotes. It also includes forms from several Gram-positive bacteria suggested to have originated from the eukaryotic form by lateral transfer. It differs in a number of biochemical properties (such as inhibition by acetyl-CoA) from most bacterial CoaA and lacks sequence similarity. This enzyme is the key regulatory step in the biosynthesis of coenzyme A (CoA). [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 273135 [Multi-domain]  Cd Length: 296  Bit Score: 324.74  E-value: 7.76e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160    20 PWFGMDIGGTLTKLVYFEPKditpdeqdreagilrnirryltknsaygktghrdthlqmdnveirkrrGSLHFIRFQTTD 99
Cdd:TIGR00555   1 SRIGIDIGGTLIKVVYEEKK------------------------------------------------GRRKFKTFETTN 32
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160   100 MGNFLSLAK-QKGMAELVTTVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFADLHNRTECYYYENArdilKSE 178
Cdd:TIGR00555  33 IDKFIEWLKnQIHRHSRITTLCATGGGAFKFAELIYESAGIQLHKFDEFDALIQGLNYLLKEEPKEKFTYYDF----ECQ 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160   179 KQQFNFSQPFPFILVNVGSGVSILAVYGpDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKDI 258
Cdd:TIGR00555 109 KKPIDLDDIYPYLLVNIGTGTSILYVDG-DNYERVGGTSLGGGTFLGLGKLLTGIQTFDELLEMAQHGDRTNVDLLVGDI 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160   259 YGGDYNRFGLPGDLVASSFGQMHLNDKRVSVSREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNPISMKL 338
Cdd:TIGR00555 188 YGGDYSESGLDGSLTASSFGKVLSKHLDQSFSPEDIAASLLGLIGNNIGQIAYLCALRYNIDRIVFIGSFLRNNQLLMKV 267
                         330       340       350
                  ....*....|....*....|....*....|.
gi 20544160   339 LAYAMEFWSngtMKGLFLEHEGYFGALGCLL 369
Cdd:TIGR00555 268 LSYATNFWS---KKALFLEHEGYSGAIGALL 295
PLN02902 PLN02902
pantothenate kinase
22-372 4.34e-69

pantothenate kinase


Pssm-ID: 215489 [Multi-domain]  Cd Length: 876  Bit Score: 234.40  E-value: 4.34e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160   22 FGMDIGGTLTKLVYFEPKDITPDEQDREagilRNIRRYLTKNSaygktGHRDTHLQMDnveirkrrGSLHFIRFQTTDMG 101
Cdd:PLN02902  56 LALDIGGSLIKLVYFSRHEDRSTDDKRK----RTIKERLGITN-----GNRRSYPILG--------GRLHFVKFETSKIN 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160  102 NFLSLAKQKGM-------------AELVTTVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFADLHNRTECYYY 168
Cdd:PLN02902 119 ECLDFISSKQLhrggihswlskapPNGNGVIKATGGGAYKFADLFKERLGVSLDKEDEMDCLVAGANFLLKAIRHEAFTH 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160  169 enardiLKSEKQ--QFNFSQPFPFILVNVGSGVSILAVYGPDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKG 246
Cdd:PLN02902 199 ------MEGEKEfvQIDQNDLFPYLLVNIGSGVSMIKVDGDGKFERVSGTNVGGGTYWGLGRLLTKCKSFDELLELSQRG 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160  247 DNRKVDKLVKDIYGG-DYNRFGLPGDLVASSFGQMHLNDKRVSVSR-EDLANATLVTITNNIGSIARMCALNEKIDRVVF 324
Cdd:PLN02902 273 DNSAIDMLVGDIYGGmDYSKIGLSASTIASSFGKVISENKELSDYRpEDISLSLLRMISYNIGQISYLNALRFGLKRIFF 352
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 20544160  325 VGNFLRVNPISMKLLAYAMEFWSNGTMKGLFLEHEGYFGALGCLLQFN 372
Cdd:PLN02902 353 GGFFIRGHAYTMDTISFAVHFWSKGEAQAMFLRHEGFLGALGAFMSYE 400
PLN02920 PLN02920
pantothenate kinase 1
24-400 1.95e-68

pantothenate kinase 1


Pssm-ID: 215498 [Multi-domain]  Cd Length: 398  Bit Score: 222.02  E-value: 1.95e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160   24 MDIGGTLTKLVYFEPKDitPDEQDREAGILRnirrylTKNSAYGKtghrdthLQMDNVEIRKRRGSLHFIRFQTTDMGNF 103
Cdd:PLN02920  23 LDIGGSLIKLVYFSRNS--GDSEDPRNDSSV------KSDGVNGR-------LHFAKFETRKINDCLEFISSNKLHHGGF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160  104 lslAKQKGMAELVTTVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFADLHNRTECYYYENArdilKSEKQQFN 183
Cdd:PLN02920  88 ---QHHENPTHDKNFIKATGGGAYKFADLFKEKLGISLDKEDEMDCLVTGANFLLKAVHHEAFTYLDG----QKEFVQID 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160  184 FSQPFPFILVNVGSGVSILAVYGPDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKDIYGG-D 262
Cdd:PLN02920 161 HNDLYPYLLVNIGSGVSMIKVDGDGKFERVSGTSVGGGTFWGLGKLLTKCKSFDELLELSHQGNNRVIDMLVGDIYGGmD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160  263 YNRFGLPGDLVASSFGQMHLNDKRVSVSR-EDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNPISMKLLAY 341
Cdd:PLN02920 241 YSKIGLSSTTIASSFGKAISDNKELEDYKpEDVARSLLRMISNNIGQISYLNALRFGLKRIFFGGFFIRGHSYTMDTISV 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 20544160  342 AMEFWSNGTMKGLFLEHEGYFGALGCLLQFNGElaaALNDGVEHSIHTESDSASEAAQT 400
Cdd:PLN02920 321 AVHFWSKGEAKAMFLRHEGFLGALGAFMSYEKH---SLDDLMVNQVVQLPVNASSGTDT 376
ASKHA_NBD_PanK-II_bac cd24085
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins ...
23-369 4.67e-54

nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins mainly from bacteria; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. The model corresponds to a group of PanK-II that is mainly from bacteria.


Pssm-ID: 466935 [Multi-domain]  Cd Length: 262  Bit Score: 180.46  E-value: 4.67e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160  23 GMDIGGTLTKLVYFEPKditpdeqdreagilrnirryltknsaygktghrdthlqmdnveirkrrGSLHFIRFQTTDMGN 102
Cdd:cd24085   3 GIDAGGTLTKIVLLENN------------------------------------------------GELKFKAFDSLKIEA 34
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 103 FLSLAKQKGMAElVTTVCATGGGAFKFEQDFrdqVNMKLAKFDELDTLIKGILFadlhnrtecyyyenardILKSEKQqf 182
Cdd:cd24085  35 LVKFLNELGIND-IEKIAVTGGGASRLPENI---DGIPIVKVDEFEAIGRGALY-----------------LLGEILD-- 91
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 183 nfsqpfPFILVNVGSGVSILAVYGpDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKDIYGGD 262
Cdd:cd24085  92 ------DALVVSIGTGTSIVLAKN-GTIRHVGGTGVGGGTLLGLGKLLLGVTDYDEITELARKGDRSNVDLTVGDIYGGG 164
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 263 YnrFGLPGDLVASSFGQMHLNDKrvsVSREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRvNPISMKLLAYA 342
Cdd:cd24085 165 I--GPLPPDLTASNFGKLADDNK---ASREDLAAALINLVGETIGTLAALAARAEGVKDIVLVGSTLR-NPLLKEVLERY 238
                       330       340
                ....*....|....*....|....*..
gi 20544160 343 MEFwsnGTMKGLFLEHEGYFGALGCLL 369
Cdd:cd24085 239 TKL---YGVKPIFPENGEFAGAIGALL 262
PTZ00297 PTZ00297
pantothenate kinase; Provisional
24-396 9.25e-44

pantothenate kinase; Provisional


Pssm-ID: 140318 [Multi-domain]  Cd Length: 1452  Bit Score: 163.87  E-value: 9.25e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160    24 MDIGGTLTKLVYFEPK--DITPDEQDREAGILRNirryltknsaygKTGHRDTHLQMD----NVEIRKRR----GSLHFI 93
Cdd:PTZ00297 1044 IDIGGTFAKIAYVQPPggFAFPTYIVHEASSLSE------------KLGLRTFHFFADaeaaESELRTRPhsrvGTLRFA 1111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160    94 RFQTTDMGNFLS-LAKQKGMA----ELVTTVCATGGGAFKFEQDFRDQVNMKLAKFDELDTLIKGILFADLHNRTECYYY 168
Cdd:PTZ00297 1112 KIPSKQIPDFADyLAGSHAINyykpQYRTKVRATGGGAFKYASVAKKVLGINFSVMREMDAVVKGLNLVIRVAPESIFTV 1191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160   169 ENARDI-----LKSEKQQfNFSqPFPFILVNVGSGVSILAVYGPD-NYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQ- 241
Cdd:PTZ00297 1192 DPSTGVhhphqLVSPPGD-GFS-PFPCLLVNIGSGISIIKCLGPDgSHVRVGGSPIGGATFWGLVRTMTNVTSWEEVMEi 1269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160   242 --LATKGDNRKVDKLVKDIYGgdYNRFGLPG----DLVASSFGQM---HLNDKRVSVSRE-------------------- 292
Cdd:PTZ00297 1270 mrLDGPGDNKNVDLLVGDIYG--YNAKDLPAmlsvDTVASTFGKLgteRFYEMMRGVSTAhfsdddaageilspkalksp 1347
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160   293 ------------------DLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNPISMKLLAYAMEFWSNGTMKGL 354
Cdd:PTZ00297 1348 tviselpvrngtkkasaiDIVRSLLNMISSNVTQLAYLHSRVQGVPNIFFAGGFVRDNPIIWSHISSTMKYWSKGECHAH 1427
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 20544160   355 FLEHEGYFGALGCllqfngelaaALNDgvehsihTESDSASE 396
Cdd:PTZ00297 1428 FLEHDGYLGALGC----------ATLD-------PDGDAASE 1452
PanK COG5146
Pantothenate kinase [Coenzyme transport and metabolism]; Pantothenate kinase is part of the ...
23-369 1.27e-40

Pantothenate kinase [Coenzyme transport and metabolism]; Pantothenate kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 444059 [Multi-domain]  Cd Length: 270  Bit Score: 145.42  E-value: 1.27e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160  23 GMDIGGTLTKLVYFEpkditpdeqdreagilrnirryltknsaygktghrdthlqmdnveirkrRGSLHFIRFQTTDMGN 102
Cdd:COG5146   5 GIDAGGTLTKIAYLE-------------------------------------------------DGERRYKKFPSDEIES 35
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 103 FLS-LAKQKGMAElvttVCATGGGAFKFEQDFRDqvnMKLAKFDELDTLIKGILFadlhnrtecyyyenardILKSEKQQ 181
Cdd:COG5146  36 VADwLNKFINIEK----IGLTGGRAEVLAEKLNG---DPKQYIVEFDATGKGVRY-----------------LLKEEGHD 91
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 182 FNfsqpfPFILVNVGSGVSILAVYGpDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKDIYGG 261
Cdd:COG5146  92 ID-----KFIITNVGTGTSIHYMDG-DTQERVGGTGVGGGTLMGLSYLLTGISDFEEIVELAKKGDRDGIDLKVKDIYEG 165
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160 262 DYNrfGLPGDLVASSFGQMHLNDKRvSVSREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNPismkLLAY 341
Cdd:COG5146 166 MEP--PIPGDLTASNFGKVLITLDE-SATKEDILAAIIGLVGETITTLSIQAAEEYDTETIVYIGSTLTNNP----LLQE 238
                       330       340       350
                ....*....|....*....|....*....|.
gi 20544160 342 AMEFWSngTMKGL---FLEHEGYFGALGCLL 369
Cdd:COG5146 239 VIESYT--ILRGKkpiFLENGEFSGAIGALL 267
PRK13317 PRK13317
pantothenate kinase; Provisional
23-371 3.25e-36

pantothenate kinase; Provisional


Pssm-ID: 237346 [Multi-domain]  Cd Length: 277  Bit Score: 133.93  E-value: 3.25e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160   23 GMDIGGTLTKLVYFEPKDItpdeqdreagilrnirRYLTknSAYGKTGHRDTHLQMDNVEIRKrrgslhfirfqttdmgn 102
Cdd:PRK13317   6 GIDAGGTLTKIVYLEEKKQ----------------RTFK--TEYSAEGKKVIDWLINLQDIEK----------------- 50
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160  103 flslakqkgmaelvttVCATGGGAFKFEQDFRDQVnmKLAKFDELDTLIKGILFadlhnrtecyyyenardILKSEKQQF 182
Cdd:PRK13317  51 ----------------ICLTGGKAGYLQQLLNYGY--PIAEFVEFEATGLGVRY-----------------LLKEEGHDL 95
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160  183 NfsqpfPFILVNVGSGVSILAVYGpDNYKRISGTSLGGGTFLGLCCLLTGCTSFEEAIQLATKGDNRKVDKLVKDIYGGD 262
Cdd:PRK13317  96 N-----DYIFTNIGTGTSIHYVDG-NSQRRVGGTGIGGGTIQGLSKLLTNISDYEQLIELAKHGDRNNIDLKVGDIYKGP 169
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20544160  263 YNrfGLPGDLVASSFGQMhLNDKRVSVSREDLANATLVTITNNIGSIARMCALNEKIDRVVFVGNFLRVNPismkLLAYA 342
Cdd:PRK13317 170 LP--PIPGDLTASNFGKV-LHHLDSEFTSSDILAGVIGLVGEVITTLSIQAAREKNIENIVYIGSTLTNNP----LLQEI 242
                        330       340       350
                 ....*....|....*....|....*....|..
gi 20544160  343 MEFWSNgtMKG---LFLEHEGYFGALGCLLQF 371
Cdd:PRK13317 243 IESYTK--LRNctpIFLENGGYSGAIGALLLA 272
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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